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1000 results found for “Regulator of Calcineurin”
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Name :
SELANKDescription:
SELANK
Product # :
HOR-035Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SELANK Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 751.89 Dalton and a Molecular formula of C33H57N11O9.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SELANK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELANK should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SELANK in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Thr-Lys-Pro-Arg-Pro-Gly-Pro-OH.
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Background
Selank, also known as TP-7, is a synthetic peptide that has garnered significant attention in the scientific community due to its potential anxiolytic, neuroprotective, and nootropic effects. This heptapeptide, derived from the naturally occurring human tetrapeptide Tuftsin, has been shown to possess a wide range of biological activities, including enhancing memory, reducing anxiety, and potentially mitigating the effects of neurodegenerative diseases.
Selank's primary mechanism of action involves its interaction with the GABAergic system, the body's main inhibitory neurotransmitter system. By modulating the activity of GABA receptors, Selank can exert a calming effect on the brain, reducing anxiety and enhancing cognitive function. Studies by Semenova et al. (2014) have demonstrated that Selank can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.
In addition to its anxiolytic and nootropic effects, Selank has been shown to possess neuroprotective properties. Research by Ershov et al. (2016) found that Selank could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its anxiolytic, nootropic, and neuroprotective effects, Selank has been proposed as a potential therapeutic agent for a variety of conditions, including anxiety disorders, cognitive disorders, and neurodegenerative diseases. For instance, a study by Medvedev et al. (2017) found that Selank could improve symptoms in patients with generalized anxiety disorder, indicating its potential as a therapeutic agent in the treatment of anxiety disorders.
While research on Selank is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of Selank in humans. However, the existing body of research suggests that Selank could be a promising tool in the treatment of anxiety disorders, cognitive disorders, and neurodegenerative diseases.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Eotaxin MouseDescription:
Eotaxin Mouse Recombinant (CCL11)
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
Product # :
CHM-308Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Eotaxin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8403.2 Dalton. The CCL11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.More Info
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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Eotaxin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be His-Pro-Gly-Ser-Ile.
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Background
What is the molecular weight/Mw of EOTAXIN MOUSE Protein?
EOTAXIN MOUSE Protein has a total Mw of 8.4kDa.
What is the source or expression system of EOTAXIN MOUSE Protein?
Escherichia Coli.
What is the Purity of EOTAXIN MOUSE Protein?
EOTAXIN MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN MOUSE Protein?
The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.
What is the amino acid sequence of EOTAXIN MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be His-Pro-Gly-Ser-Ile.
What applications can EOTAXIN MOUSE Protein be used in?
EOTAXIN MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN MOUSE Protein?
The endotoxin level is minimal, EOTAXIN MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ACE2 MouseDescription:
Angiotensin Converting Enzyme 2 Mouse Recombinant
ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.
Product # :
ENZ-1123Price :
Quantity :
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Shipped with Ice Packs
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Description
ACE2 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 731 amino acids (18-740 aa) and having a molecular mass of 84.5kDa. ACE2 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The ACE2 solution contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Greater than 200pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1 pmole of McaYVADAPK(Dnp)-OH per min. at pH-7.5, at 25C.
More Info
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Introduction
ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.
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Synonyms
ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
QSLTEENAKT FLNNFNQEAE DLSYQSSLAS WNYNTNITEE NAQKMSEAAA KWSAFYEEQS KTAQSFSLQE IQTPIIKRQL QALQQSGSSA LSADKNKQLN TILNTMSTIY STGKVCNPKN PQECLLLEPG LDEIMATSTD YNSRLWAWEG WRAEVGKQLR PLYEEYVVLK NEMARANNYN DYGDYWRGDY EAEGADGYNY NRNQLIEDVE RTFAEIKPLY EHLHAYVRRK LMDTYPSYIS PTGCLPAHLL GDMWGRFWTN LYPLTVPFAQ KPNIDVTDAM MNQGWDAERI FQEAEKFFVS VGLPHMTQGF WANSMLTEPA DGRKVVCHPT AWDLGHGDFR IKMCTKVTMD NFLTAHHEMG HIQYDMAYAR QPFLLRNGAN EGFHEAVGEI MSLSAATPKH LKSIGLLPSD FQEDSETEIN FLLKQALTIV GTLPFTYMLE KWRWMVFRGE IPKEQWMKKW WEMKREIVGV VEPLPHDETY CDPASLFHVS NDYSFIRYYT RTIYQFQFQE ALCQAAKYNG SLHKCDISNS TEAGQKLLKM LSLGNSEPWT KALENVVGAR NMDVKPLLNY FQPLFDWLKE QNRNSFVGWN TEWSPYADQS IKVRISLKSA LGANAYEWTN NEMFLFRSSV AYAMRKYFSI IKNQTVPFLE EDVRVSDLKP RVSFYFFVTS PQNVSDVIPR SEVEDAIRMS RGRINDVFGL NDNSLEFLGI HPTLEPPYQPPVTLEHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
S100A3 HumanDescription:
S100 Calcium Binding Protein A3 Human Recombinant
S100-A3, S-100E, S100 calcium-binding protein A3, S100E, S-100A3, Protein S100-A3, Protein S-100E, S100A3.
Product # :
PRO-755Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.9kDa.The S100A3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A3 protein at 1mg/ml in 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.2M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.
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Synonyms
S100-A3, S-100E, S100 calcium-binding protein A3, S100E, S-100A3, Protein S100-A3, Protein S-100E, S100A3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MARPLEQAVA AIVCTFQEYA GRCGDKYKLC QAELKELLQK ELATWTPTEF RECDYNKFMS VLDTNKDCEV DFVEYVRSLA CLCLYCHEYF KDCPSEPPCS Q.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CST6 HumanDescription:
Cystatin E/M Human Recombinant
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
Product # :
PRO-892Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CST6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (29-149) and having a molecular mass of 15.9 kDa.The CST6 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CST6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CST6 belongs to the type 2 cystatin family. Unlike other family members that act as active cysteine protease inhibitors, CST6 restrain the inhibition of cathepsin B but is not active against cathepsin C. CST6 are secretable proteins that influence osteogenesis and bone resorption, regulation of the hepatocyte growth factor receptors, and the response to systemic inflammation.
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Synonyms
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRPQERMVGE LRDLSPDDPQ VQKAAQAAVA SYNMGSNSIY YFRDTHIIKA QSQLVAGIKY FLTMEMGSTD CRKTRVTGDH VDLTTCPLAA GAQQEKLRCD FEVLVVPWQN SSQLLKHNCV QM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Adiponectin Human, HMWDescription:
Adiponectin glycosylated Human Recombinant, HMW Rich
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-764Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.
Source
HEK293.
Formulation
Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
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Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.6 kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ARG2 HumanDescription:
Arginase Type II Human Recombinant
Kidney Arginase, Non-Hepatic Arginase, EC 3.5.3.1, Arginase-2, Type II arginase, Kidney-type arginase, Arginase-2 mitochondrial.
Product # :
ENZ-526Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARG2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (23-354 a.a.) and having a molecular mass of 38.3 kDa. The ARG2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARG2 Human solution containing 20mM Tris-HCl pH-8, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ARG2 participates in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, ARG2 takes part in both male and female sexual arousal and therefore a potential target for the treatment of male and female sexual arousal disorders.
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Synonyms
Kidney Arginase, Non-Hepatic Arginase, EC 3.5.3.1, Arginase-2, Type II arginase, Kidney-type arginase, Arginase-2 mitochondrial.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVHSVAVIGA PFSQGQKRKG VEHGPAAIRE AGLMKRLSSL GCHLKDFGDL SFTPVPKDDL YNNLIVNPRS VGLANQELAE VVSRAVSDGY SCVTLGGDHS LAIGTISGHA RHCPDLCVVW VDAHADINTP LTTSSGNLHG QPVSFLLREL QDKVPQLPGF SWIKPCISSA SIVYIGLRDV DPPEHFILKN YDIQYFSMRD IDRLGIQKVM ERTFDLLIGK RQRPIHLSFD IDAFDPTLAP ATFTPVVGGL TYREGMYIAE EIHNTGLLSA LDLVEVNPQL ATSEEEAKTT ANLAVDVIAS SFGQTREGGH IVYDQLPTPS SPDESENQAR VRI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 22 MouseDescription:
Interleukin-22 Mouse Recombinant
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Product # :
CYT-539Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids and having a molecular mass of 16.7 kDa. The Murine IL-22 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 1X PBS.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by its ability to induce IL-10 secretion in Colo205 cells is less than 0.5ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.More Info
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Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10R? (previously known as CRF2-4), belonging to the class II cytokine receptor family.
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Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin -22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Pro-Val-Asn.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
C5a MouseDescription:
Complement Component C5a Mouse Recombinant
Complement C5, Hemolytic complement, C5, Hc, He, C5a.
Product # :
PRO-085Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C5a Mouse Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9kDa.The Mouse C5a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Mouse C5a was lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.5 and 350mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 of Recombinant Mouse C5a as determined by its ability to induce N-acetyl-b-D-glucosaminidase release from differentiated U937 human histiocytic lymphoma cells was 5-20ng/ml.More Info
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Introduction
Mouse Complement 5a (C5a) is a glycoprotein which is a member of a family of structurally and functionally related proteins known as anaphylatoxins. C5a is a 77 a.a. peptide created by the C5a convertase proteolytic cleavage of C5 ? chain in the classical and alternative complement pathway (C4b2a3b, C3bBb3b). The mouse C5a has four ? helices and three intrachain disulfide bonds which form a triple loop structure. C5a functions through G-protein coupled receptor (GPCR) (C5aR/CD88). C5a is a effective chemoattractant and anaphylatoxin which functions on all classes of leukocytes and on many other cell types including endothelial, smooth muscle, kidney, liver, and neural cells. Mouse C5a also mediates IL-8 release from bronchial epithelial cells. Furthermore, it triggers an oxidative surge in macrophages and neutrophils, causing the release of histamine in basophils and mast cells. The C5a anaphylatoxin activity on hepatocytes results indirectly from interaction with nonparenchymal cell via prostanoid secretion.
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Synonyms
Complement C5, Hemolytic complement, C5, Hc, He, C5a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse C5a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse C5a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Mouse C5a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Leu-His-Leu-Leu.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FGF8 Human, HEKDescription:
Fibroblast Growth Factor-8 Human Recombinant, HEK
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Product # :
CYT-087Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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- More Info
Description
FGF-8 Human Recombinant is a single, glycosylated, polypeptide chain (23-215 a.a) containing a total of 204 amino acids and having a molecular mass of 23.7 kDa. FGF-8 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The FGF-8 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90% as obsereved by SDS-PAGE.
Biological Activity
The ED50 is ≤5 µg/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.
More Info
-
Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
-
Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.
-
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 23.7kDa.
What is the source or expression system of FGF8 Protein?
HEK.
What is the Purity of FGF8 Protein?
FGF8 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF8 Protein?
The ED50 is ≤5 µg/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.
What is the amino acid sequence of FGF8 Protein?
DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.
What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Follistatin Human, HisDescription:
Follistatin Human Recombinant, His Tag
FST, FS, Activin-binding protein.
Product # :
CYT-029Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
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- More Info
Description
FST His Protein is 36.0 kDa protein containing 325 amino acid residues of the FST His and the 10 aa N-Terminal His-tag.
Source
E. coli.
Formulation
FST His Tag was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.
More Info
-
Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
-
Synonyms
FST, FS, Activin-binding protein.
-
Stability
Store lyophilized FST His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted FST His can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
-
Amino Acid Sequence
MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.
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Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN, HIS Protein?
FOLLISTATIN HUMAN, HIS Protein has a total Mw of 36kDa.
What is the source or expression system of FOLLISTATIN HUMAN, HIS Protein?
Escherichia Coli.
What is the Biological Activity of FOLLISTATIN HUMAN, HIS Protein?
The biological functionality of FOLLISTATIN HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of FOLLISTATIN HUMAN, HIS Protein?
MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.
What applications can FOLLISTATIN HUMAN, HIS Protein be used in?
FOLLISTATIN HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN, HIS Protein?
The endotoxin level is minimal, FOLLISTATIN HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GTF2A1 HumanDescription:
General Transcription Factor IIA, 1 Human Recombinant
General transcription factor IIA, 1, 19/37kDa, TF2A1, TFIIA, TFIIA-42, TFIIAL, Transcription initiation factor IIA subunit 1, Transcription initiation factor TFIIA 42 kDa subunit, GTF2A1.
Product # :
PRO-1808Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
GTF2A1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 297 amino acids (1-274) and having a molecular mass of 32.2kDa. GTF2A1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GTF2A1 solution (0.5mg/ml) contains 20mM Tris-HCl(pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
General Transcription Factor IIA, 1 (GTF2A1) in a complex along with TBP mediates transcriptional activity. GTF2A1 is a part of the transcription machinery of RNA polymerase II and is also participates in transcriptional activation.
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Synonyms
General transcription factor IIA, 1, 19/37kDa, TF2A1, TFIIA, TFIIA-42, TFIIAL, Transcription initiation factor IIA subunit 1, Transcription initiation factor TFIIA 42 kDa subunit, GTF2A1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMANSANT NTVPKLYRSV IEDVINDVRD IFLDDGVDEQ VLMELKTLWE NKLMQSRAVD GFHSEEQQLL LQVQQQHQPQ QQQHHHHHHH QQAQPQQTVP QQAQTQQVLI PASQQATAPQ VIVPDSKLIQ HMNASNMSAA ATAATLALPA GVTPVQQILT NSGQLLQVVR AANGAQYIFQ PQQSVVLQQQ VIPQMQPGGV QAPVIQQVLA PLPGGISPQT GVIIQPQQIL FTGNKTQVIP TTVAAPTPAQ AQITATGQQQ PQAQPAQTQA PLVLQVD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BNP Human, HisDescription:
B-type Natriuretic Peptide Human Recombinant, His Tag
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Product # :
CYT-605Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
BNP Recombinant Human fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids (27-134 a.a) and having a molecular mass of 14 kDa. BNP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BNP 0.5mg/ml is formulated with 1X PBS pH-7.4, 2mM DTT, 0.1mM PMSF, 1mM EDTA and 40% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
sds-page
More Info
-
Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
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Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHPLGSPGSA SDLETSGLQE QRNHLQGKLSELQVEQTSLE PLQESPRPTG VWKSREVATE GIRGHRKMVL YTLRAPRSPK MVQGSGCFGR KMDRISSSSG LGCKVLRRH.
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Background
What is the molecular weight / Mw of BNP His Protein?
BNP Protein has a total Mw of 14kDa.
What is the source or expression system of BNP His Protein?
Escherichia Coli.
What is the Purity of BNP His Protein?
BNP Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BNP His Protein?
The biological functionality of BNP His Protein will be determined in the future.
What is the amino acid sequence of BNP His Protein?
MGSSHHHHHH SSGLVPRGSH MHPLGSPGSA SDLETSGLQE QRNHLQGKLSELQVEQTSLE PLQESPRPTG VWKSREVATE GIRGHRKMVL YTLRAPRSPK MVQGSGCFGR KMDRISSSSG LGCKVLRRH
What applications can BNP His Protein be used in?
BNP Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BNP His Protein?
The endotoxin level is minimal, BNP His Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CTF1 RatDescription:
Cardiotrophin-1 Rat Recombinant
Cardiotrophin-1, CT-1, Ctf1.
Product # :
CYT-199Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.More Info
-
Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
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Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.
What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 1 beta RatDescription:
Interleukin-1 beta Rat Recombinant
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
CYT-394Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Interleukin-1b Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17.3 kDa.The IL-1b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 0.2um filtered concentrated solution in PBS, pH 7.4, 5% trehalose and 0.02 % Tween-20.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Biological Activity
The ED50 was found to be less than 0.1ng/ml, determined by the dose dependent proliferation of mouse D10S cells, corresponding to a specific activity of 10,000,000 units/mg.More Info
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Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.
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Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1b should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Interleukin 1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MVPIRQLHCRLRDEQQKCLVLSDPCELKALHLNGQNISQQVVFSMSF
VQGETSNDKIPVALGLKGLNLYLSCVMKDGTPTLQLESVDPKQYPKK
KMEKRFVFNKIEVKTKVEFESAQFPNWYISTSQAEHRPVFLGNSNGRD
IVDFTMEPVSS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 21 RatDescription:
Interleukin-21 Rat Recombinant
Interleukin-21, IL-21, Il21.
Product # :
CYT-033Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Interleukin-21 Rat Recombinant produced in E.Coli is a single, non-glycosilated polypeptide chain containing 129 amino acids and having a total molecular mass of 15.2kDa. The Rat IL-21 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Rat IL-21 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity is measured by its ability to proliferate activated B cells.More Info
-
Introduction
IL-21 is produced by CD4+ T cells in response to antigenic stimulation. Its action enhances antigen-specific responses of immune cells. The biological effects of IL-21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation (in conjuction) with IL-4 of IgG production, and induction of apoptotic effects in naive B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the gamma chain (°C) found in other cytokine receptors including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.
-
Synonyms
Interleukin-21, IL-21, Il21.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Rat IL-21 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL21 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Rat IL21 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
HKSSPQRPDH LLIRLRHLMD IVEQLKIYEN DLDPELLTAP QDVKGQCEHE AFACFQKAKL KPSNTGNNKT FINDLLAQLR RRLPAKRTGN KQRHMAKCPS CDLYEKKTPK EFLERLKWLL QKMIHQHLS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL15RA HumanDescription:
Interleukin 15 Receptor Alpha, Recombinant Human
Interleukin 15 Receptor Subunit Alpha, Interleukin 15 Receptor, Alpha, Interleukin 15 Receptor Alpha Isoform EM2, Interleukin 15 Receptor Alpha Isoform IC2, Interleukin 15 Receptor Alpha Isoform IC3, Interleukin 15 Receptor Alpha Isoform IC4, Interleukin 15 Receptor Alpha Isoform IC5, Interleukin 15 Receptor Alpha Isoform IC6, Interleukin 15 Receptor Alpha Isoform IC7,Interleukin 15 Receptor Alpha Isoform IC8, Interleukin-15 Receptor Subunit Alpha, IL-15 Receptor Subunit Alpha, CD215 Antigen, IL-15R-Alpha, IL-15RA, CD215.
Product # :
CYT-1037Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
IL15RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (31-205 a.a.) and fused to a 242 a.a. hIgG-His Tag at C-terminus containing a total of 417 amino acids and having a molecular mass of 45.6kDa.IL15RA shows multiple bands between 57-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL15RA protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Determined by its ability to inhibit proliferation using CTLL2 mouse cytotoxic T cells. The ED50 for this effect is < 2 ng/ml with Human IL-15.
More Info
-
Introduction
IL15RA, also known as Interleukin 15 Receptor Alpha, is a high-affinity receptor for interleukin-15. IL15RA plays a role as a heterotrimer with the IL-2 receptor beta and gamma subunits to commence signal transduction. IL15/IL15R alpha complexes can transmit reverse signaling which promotes cellular adhesion, tyrosine phosphorylation of intracellular proteins, as well as cytokine secretion by the IL‑15/IL15R alpha expressing cells.
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Synonyms
Interleukin 15 Receptor Subunit Alpha, Interleukin 15 Receptor, Alpha, Interleukin 15 Receptor Alpha Isoform EM2, Interleukin 15 Receptor Alpha Isoform IC2, Interleukin 15 Receptor Alpha Isoform IC3, Interleukin 15 Receptor Alpha Isoform IC4, Interleukin 15 Receptor Alpha Isoform IC5, Interleukin 15 Receptor Alpha Isoform IC6, Interleukin 15 Receptor Alpha Isoform IC7,Interleukin 15 Receptor Alpha Isoform IC8, Interleukin-15 Receptor Subunit Alpha, IL-15 Receptor Subunit Alpha, CD215 Antigen, IL-15R-Alpha, IL-15RA, CD215.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADPITCPPPM SVEHADIWVK SYSLYSRERY ICNSGFKRKA GTSSLTECVL NKATNVAHWT TPSLKCIRDP ALVHQRPAPP STVTTAGVTP QPESLSPSGK EPAASSPSSN NTAATTAAIV PGSQLMPSKS PSTGTTEISS HESSHGTPSQ TTAKNWELTA SASHQPPGVY PQGHSDTTLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL1RL1 HumanDescription:
Interleukin-1 receptor-like 1 Human Recombinant
Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.
Product # :
CYT-671Price :
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Description
IL1RL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 310 amino acids fragment (19-328) corresponding to the soluble IL1RL1 coding sequence, having a molecular weight of 39.5kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL1RL1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL1RL1 protein solution is supplied in 25mM Sodium Acetate pH 4.8 and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.
A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.
Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells. -
Synonyms
Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL5RA MouseDescription:
Interleukin-5 Receptor Alpha Mouse Recombinant
Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA, CD125.
Product # :
CYT-955Price :
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Description
IL5RA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 330 amino acids (18-339a.a.) and having a molecular mass of 37.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). IL5RA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL5RA protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-5 receptor subunit alpha (Il5ra) regulates the development and function of eosinophils. The Il5ra protein is a therapeutic target for hypereosinophilic diseases including allergic inflammations and asthma. Oct2 enhances antibody-secreting cell differentiation via regulation of Il5ra chain expression on activated B cells.
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Synonyms
Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA, CD125.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
DLLNHKKFLL LPPVNFTIKA TGLAQVLLHW DPNPDQEQRH VDLEYHVKIN APQEDEYDTR KTESKCVTPL HEGFAASVRT ILKSSHTTLA SSWVSAELKA PPGSPGTSVT NLTCTTHTVV SSHTHLRPYQ VSLRCTWLVG KDAPEDTQYF LYYRFGVLTE KCQEYSRDAL NRNTACWFPR TFINSKGFEQ LAVHINGSSK RAAIKPFDQL FSPLAIDQVN PPRNVTVEIE SNSLYIQWEK PLSAFPDHCF NYELKIYNTK NGHIQKEKLI ANKFISKIDD VSTYSIQVRA AVSSPCRMPG RWGEWSQPIY VGKERKSLVE WHLEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL6R MouseDescription:
IL-6 Receptor Beta Mouse Recombinant
IL-6 receptor subunit beta, IL-6R subunit beta, IL-6R-beta, IL-6RB, Interleukin-6 signal transducer, Membrane glycoprotein 130, gp130, Oncostatin-M receptor subunit alpha,CD130.
Product # :
CYT-918Price :
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Description
IL6R produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 603 amino acids (23-617a.a.) and having a molecular mass of 67.7kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).IL6R is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
IL6R protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The IL-6 receptor complex is composed of two membrane glycoproteins: the low affinity receptor and the signaltransducing component. The soluble form of IL6R is found in the urine of healthy adult humans and the serum of HIV positive individuals, as well as in the cell culture supernatants of stimulated PBMC’s. This soluble form of IL6R results from either proteolytic cleavage from the membrane, or an isoform derived splice variant.
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Synonyms
IL-6 receptor subunit beta, IL-6R subunit beta, IL-6R-beta, IL-6RB, Interleukin-6 signal transducer, Membrane glycoprotein 130, gp130, Oncostatin-M receptor subunit alpha,CD130.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
QLLEPCGYIY PEFPVVQRGS NFTAICVLKE ACLQHYYVNA SYIVWKTNHA AVPREQVTVI NRTTSSVTFT DVVLPSVQLT CNILSFGQIE QNVYGVTMLS GFPPDKPTNL TCIVNEGKNM LCQWDPGRET YLETNYTLKS EWATEKFPDC QSKHGTSCMV SYMPTYYVNI EVWVEAENAL GKVSSESINF DPVDKVKPTP PYNLSVTNSE ELSSILKLSW VSSGLGGLLD LKSDIQYRTK DASTWIQVPL EDTMSPRTSF TVQDLKPFTE YVFRIRSIKD SGKGYWSDWS EEASGTTYED RPSRPPSFWY KTNPSHGQEY RSVRLIWKAL PLSEANGKIL DYEVILTQSK SVSQTYTVTG TELTVNLTND RYVASLAARN KVGKSAAAVL TIPSPHVTAA YSVVNLKAFP KDNLLWVEWT PPPKPVSKYI LEWCVLSENA PCVEDWQQED ATVNRTHLRG RLLESKCYQI TVTPVFATGP GGSESLKAYL KQAAPARGPT VRTKKVGKNE AVLAWDQIPV DDQNGFIRNY SISYRTSVGK EMVVHVDSSH TEYTLSSLSS DTLYMVRMAA YTDEGGKDGP EFTFTTPKFA QGEIELEHHH HHH.
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Background
Research Paper on IL-6 Receptor Beta Mouse Recombinant
Abstract:
The IL-6 Receptor Beta Mouse Recombinant stands as a pivotal player in deciphering the intricate realm of immune modulation. This research paper offers an in-depth exploration of its molecular intricacies and its profound implications in immunological research. By delving into its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its role in shaping immune responses.
Introduction:
The IL-6 Receptor Beta Mouse Recombinant has emerged as a central focus in immunological investigations. This paper aims to provide a comprehensive understanding of its molecular attributes and its influence on immune mechanisms.
Molecular Insights and Signaling Proficiency:
Examining the molecular architecture of IL-6 Receptor Beta Mouse Recombinant, we uncover its critical role in transducing IL-6 signals. Its intricate interactions and signaling proficiency contribute to precise immune responses.
Influencing Immune Responses:
IL-6, a key cytokine, exerts remarkable effects on immune cell activation and inflammation. IL-6 Receptor Beta Mouse Recombinant serves as an essential component in the IL-6 signaling pathway, influencing immune outcomes.
Synonyms and Network Connections:
Understanding the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2, deepens our comprehension of cytokine-mediated signaling networks. The intricate interplay between IL-6 Receptor Beta Mouse Recombinant and these molecules shapes immune dynamics.
Potential Therapeutic and Research Applications:
IL-6 Receptor Beta Mouse Recombinant transcends the boundaries of laboratory research. Its potential as a therapeutic target for immune-related disorders and its utility in deciphering immune responses offer promising avenues for clinical applications.
Clinical Relevance and Future Prospects:
The clinical relevance of IL-6 Receptor Beta Mouse Recombinant is highlighted by its role in diseases characterized by dysregulated IL-6 signaling. Exploring its therapeutic potential paves the way for novel strategies to modulate immune-related conditions.
Conclusion:
In the intricate tapestry of immunology, IL-6 Receptor Beta Mouse Recombinant emerges as a central player in orchestrating immune responses. Its molecular intricacies, pivotal functions, and potential therapeutic implications position it as a cornerstone in understanding immune regulation and developing innovative interventions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TMOD3 HumanDescription:
Tropomodulin 3 Human Recombinant
Tropomodulin-3, Ubiquitous tropomodulin, U-Tmod, TMOD3, UTMOD.
Product # :
PRO-1165Price :
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Description
TMOD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (1-352 a.a) and having a molecular mass of 42kDa.TMOD3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TMOD3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Tropomodulin 3 (TMOD3) is a member of the tropomodulin family. TMOD3 prevents the elongation and depolymerization of the actin filaments at the pointed end. Actin cytoskeleton regulation by filament capping proteins is essential to many dynamic cellular functions. TMOD3 functions as a negative regulator of cell migration; nevertheless the processes behind its cellular functions are unknown. The Tmod/TM complex influences the formation of the short actin protofilament, which sequentially outlines the geometry of the membrane skeleton.
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Synonyms
Tropomodulin-3, Ubiquitous tropomodulin, U-Tmod, TMOD3, UTMOD.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMALPFR KDLEKYKDLD EDELLGNLSE TELKQLETVL DDLDPENALL PAGFRQKNQT SKSTTGPFDR EHLLSYLEKE ALEHKDREDY VPYTGEKKGK IFIPKQKPVQ TFTEEKVSLD PELEEALTSA SDTELCDLAA ILGMHNLITN TKFCNIMGSS NGVDQEHFSN VVKGEKILPV FDEPPNPTNV EESLKRTKEN DAHLVEVNLN NIKNIPIPTL KDFAKALETN THVKCFSLAA TRSNDPVATA FAEMLKVNKT LKSLNVESNF ITGVGILALI DALRDNETLA ELKIDNQRQQ LGTAVELEMA KMLEENTNIL KFGYQFTQQG PRTRAANAIT KNNDLVRKRR VEGDHQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CEA HumanDescription:
Carcinoembryonic Antigen Human Recombinant
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
Product # :
PRO-287Price :
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Description
CEA Human Recombinant is glycosylated with N-linked sugars and produced using baculovirus vectors in insect cells. CEA is a well-known tumor marker corresponding to the full length human CEA which is approximately 120,000 Dalton.
Source
Baculovirus Insect Cells.
Formulation
The sterile protein solution contains 10mM NaH2PO4, pH 7 and 150mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed. -
Synonyms
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
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Physical Appearance
Sterile Filtered colourless solution.
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Stability
CEA should be stored at 2-8°C.Avoid freezing.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PRLR Human, AntagonistDescription:
Prolactin Receptor Antagonist Human Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-1254Price :
Quantity :
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Shipped at Room temp
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Description
Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.
Biological Activity
fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).
More Info
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PRLR in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr
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Background
Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CNTF HumanDescription:
Ciliary-Neurotrophic Factor Human Recombinant
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-272Price :
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Shipped at Room temp
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Description
Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized HCNTF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Phe-Thr-Glu.
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Background
Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications
Abstract:
Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.
Introduction:
CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.
Mechanisms of Action:
CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.
Production Methods:
Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.
Therapeutic Applications:
CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.
Challenges and Future Directions:
While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.
Conclusion:
Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.
What is the amino acid sequence of CNTF Protein?
CNTF Protein is composed from 199 amino acids.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography techniques.
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Protein content
CNTF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of CNTF Recombinant as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.